Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone

From the marine-derived fungus Penicillium sumatrense (Trichocomaceae), a pair of enantiomers [(+)-1 and (−)-1] were isolated with identical 1D NMR data to drazepinone, which was originally reported to have a trisubstituted naphthofuroazepinone skeleton. In this study, we confirmed the structures of...

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Autores principales: Cao, Fei, Pan, Li, Gao, Wenbin, Liu, Yunfeng, Zheng, Caijuan, Zhang, Yahui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8708580/
https://www.ncbi.nlm.nih.gov/pubmed/34940713
http://dx.doi.org/10.3390/md19120714
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author Cao, Fei
Pan, Li
Gao, Wenbin
Liu, Yunfeng
Zheng, Caijuan
Zhang, Yahui
author_facet Cao, Fei
Pan, Li
Gao, Wenbin
Liu, Yunfeng
Zheng, Caijuan
Zhang, Yahui
author_sort Cao, Fei
collection PubMed
description From the marine-derived fungus Penicillium sumatrense (Trichocomaceae), a pair of enantiomers [(+)-1 and (−)-1] were isolated with identical 1D NMR data to drazepinone, which was originally reported to have a trisubstituted naphthofuroazepinone skeleton. In this study, we confirmed the structures of the two enantiomers as drazepinone and revised their structures by detailed analysis of extensive 2D NMR data and a comparison of the calculated (13)C chemical shifts, ECD, VCD, and ORD spectra with those of the experiment ones. (+)-1 and (−)-1 were evaluated for their PTP inhibitory activity in vitro. (−)-1 showed selective PTP inhibitory activity against PTP1B and TCPTP with IC(50) values of 1.56 and 12.5 μg/mL, respectively.
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spelling pubmed-87085802021-12-25 Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone Cao, Fei Pan, Li Gao, Wenbin Liu, Yunfeng Zheng, Caijuan Zhang, Yahui Mar Drugs Article From the marine-derived fungus Penicillium sumatrense (Trichocomaceae), a pair of enantiomers [(+)-1 and (−)-1] were isolated with identical 1D NMR data to drazepinone, which was originally reported to have a trisubstituted naphthofuroazepinone skeleton. In this study, we confirmed the structures of the two enantiomers as drazepinone and revised their structures by detailed analysis of extensive 2D NMR data and a comparison of the calculated (13)C chemical shifts, ECD, VCD, and ORD spectra with those of the experiment ones. (+)-1 and (−)-1 were evaluated for their PTP inhibitory activity in vitro. (−)-1 showed selective PTP inhibitory activity against PTP1B and TCPTP with IC(50) values of 1.56 and 12.5 μg/mL, respectively. MDPI 2021-12-20 /pmc/articles/PMC8708580/ /pubmed/34940713 http://dx.doi.org/10.3390/md19120714 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Cao, Fei
Pan, Li
Gao, Wenbin
Liu, Yunfeng
Zheng, Caijuan
Zhang, Yahui
Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title_full Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title_fullStr Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title_full_unstemmed Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title_short Structure Revision and Protein Tyrosine Phosphatase Inhibitory Activity of Drazepinone
title_sort structure revision and protein tyrosine phosphatase inhibitory activity of drazepinone
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8708580/
https://www.ncbi.nlm.nih.gov/pubmed/34940713
http://dx.doi.org/10.3390/md19120714
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